RMND5A, GID2A,Geenin normaalius on meiossissa ja hermostonkehitykselle tärkeä.

https://www.ncbi.nlm.nih.gov/gene/64795

Also known as

CTLH; GID2; RMD5; GID2A; p44CTLH

Expression

Ubiquitous expression in esophagus (RPKM 17.5), heart (RPKM 16.4) and 25 other tissues See more

Orthologs mouse

Preferred Names

E3 ubiquitin-protein transferase RMND5A

Names

44-kD protein coding for CTLH motif

C-terminal to LisH motif, 44 kDa

GID complex subunit 2 homolog A

protein RMD5 homolog A

NP_073617.1

• EC 2.3.2.27

Related articles in PubMed

1. Novel neurodevelopmental disorder in the case of a giant occipitoparietal meningoencephalocele. Vogel TW, et al. J Neurosurg Pediatr, 2012 Jul. PMID 22681319
2. MiR-138 downregulates miRNA processing in HeLa cells by targeting RMND5A and decreasing Exportin-5 stability. Li J, et al. Nucleic Acids Res, 2014 Jan. PMID 24057215, Free PMC Article
3. Molecular phylogeny of a RING E3 ubiquitin ligase, conserved in eukaryotic cells and dominated by homologous components, the muskelin/RanBPM/CTLH complex. Francis O, et al. PLoS One, 2013. PMID 24143168, Free PMC Article  (Molekulaarista  E3 ligaasi fylogeniaa) 
4. RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat proteins ARMC8alpha and ARMC8beta are components of the CTLH complex. Kobayashi N, et al. Gene, 2007 Jul 15. PMID 17467196
5. ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs. Bowzard JB, et al. J Biol Chem, 2007 Jun 15. PMID 17452337

See all (25) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

GeneRIFs: Gene References Into Functions

1. The study identifies a miR-138-RMND5A-Exportin-5 as a previously unknown miRNA processing regulatory pathway in HeLa cells.  (Suom. RMND5A vaikuttaa Exportiini-5:n stabiliteetti). 
2. Duplications of this region involving RMND5A, whose product contains a C-terminal to lis homology (LisH) domain, have not previously been associated with a defined phenotype but may present insight into encephalocele formation. (Suom. geeniduplikaatio  Kr. 2p11.2 aiheuttaa  RMD5A produktin  C-terminaalin LisH  suhteen  fenotyypin enkefalocoele). 
3. RanBPM, ARMC8alpha, ARMC8beta, Muskelin, p48EMLP, and p44CTLH form complexes in cells.

Submit: New GeneRIF Correction

1. NM_022780.4 → NP_073617.1  E3 ubiquitin-protein transferase RMND5A
   See identical proteins and their annotated locations for NP_073617.1
   
   Status: VALIDATED

   Source sequence(s)

   AC064848, AK023972, BC012165, BC047668, BU620245

   Consensus CDS

   CCDS1991.1

   UniProtKB/Swiss-Prot

   Q9H871

   Related

   ENSP00000283632.4, OTTHUMP00000160759, ENST00000283632.4

   Conserved Domains (3) summary

   smart00667
   Location:114 → 146

   LisH; Lissencephaly type-1-like homology motif

   pfam10607
   Location:153 → 297

   CLTH; CTLH/CRA C-terminal to LisH motif domain

   cd16794
   Location:333 → 381

   dRING_RMD5A; Degenerated RING finger found in protein RMD5 homolo

E3 ubiquitin-protein transferase RMND5A [Homo sapiens]

NCBI Reference Sequence: NP_073617.1

Identical Proteins FASTA Graphics

Go to:

LOCUS       NP_073617                391 aa            linear   PRI 23-NOV-2018
DEFINITION  E3 ubiquitin-protein transferase RMND5A [Homo sapiens].
ACCESSION   NP_073617
VERSION     NP_073617.1
DBSOURCE    REFSEQ: accession NM_022780.4
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 391)
  AUTHORS   Lampert F, Stafa D, Goga A, Soste MV, Gilberto S, Olieric N,
            Picotti P, Stoffel M and Peter M.
  TITLE     The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell
            proliferation and targets the transcription factor Hbp1 for
            degradation
  JOURNAL   Elife 7, e35528 (2018)
   PUBMED   29911972
  REMARK    Publication Status: Online-Only
REFERENCE   2  (residues 1 to 391)
  AUTHORS   Boldt K, van Reeuwijk J, Lu Q, Koutroumpas K, Nguyen TM, Texier Y,
            van Beersum SE, Horn N, Willer JR, Mans DA, Dougherty G, Lamers IJ,
            Coene KL, Arts HH, Betts MJ, Beyer T, Bolat E, Gloeckner CJ,
            Haidari K, Hetterschijt L, Iaconis D, Jenkins D, Klose F, Knapp B,
            Latour B, Letteboer SJ, Marcelis CL, Mitic D, Morleo M, Oud MM,
            Riemersma M, Rix S, Terhal PA, Toedt G, van Dam TJ, de Vrieze E,
            Wissinger Y, Wu KM, Apic G, Beales PL, Blacque OE, Gibson TJ,
            Huynen MA, Katsanis N, Kremer H, Omran H, van Wijk E, Wolfrum U,
            Kepes F, Davis EE, Franco B, Giles RH, Ueffing M, Russell RB and
            Roepman R.
  CONSRTM   UK10K Rare Diseases Group
  TITLE     An organelle-specific protein landscape identifies novel diseases
            and molecular mechanisms
  JOURNAL   Nat Commun 7, 11491 (2016)
   PUBMED   27173435
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 391)
  AUTHORS   Li J, Chen Y, Qin X, Wen J, Ding H, Xia W, Li S, Su X, Wang W, Li
            H, Zhao Q, Fang T, Qu L and Shao N.
  TITLE     MiR-138 downregulates miRNA processing in HeLa cells by targeting
            RMND5A and decreasing Exportin-5 stability
  JOURNAL   Nucleic Acids Res. 42 (1), 458-474 (2014)
   PUBMED   24057215
  REMARK    GeneRIF: The study identifies a miR-138-RMND5A-Exportin-5 as a
            previously unknown miRNA processing regulatory pathway in HeLa
            cells.
REFERENCE   4  (residues 1 to 391)
  AUTHORS   Francis O, Han F and Adams JC.
  TITLE     Molecular phylogeny of a RING E3 ubiquitin ligase, conserved in
            eukaryotic cells and dominated by homologous components, the
            muskelin/RanBPM/CTLH complex
  JOURNAL   PLoS ONE 8 (10), e75217 (2013)
   PUBMED   24143168
  REMARK    Erratum:[PLoS One. 2013 Nov 8;8(11):null. PMID: 29161723]
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 391)
  AUTHORS   Vogel TW, Manjila S and Cohen AR.
  TITLE     Novel neurodevelopmental disorder in the case of a giant
            occipitoparietal meningoencephalocele
  JOURNAL   J Neurosurg Pediatr 10 (1), 25-29 (2012)
   PUBMED   22681319
  REMARK    GeneRIF: Duplications of this region involving RMND5A, whose
            product contains a C-terminal to lis homology (LisH) domain, have
            not previously been associated with a defined phenotype but may
            present insight into encephalocele formation.
REFERENCE   6  (residues 1 to 391)
  AUTHORS   Kobayashi N, Yang J, Ueda A, Suzuki T, Tomaru K, Takeno M, Okuda K
            and Ishigatsubo Y.
  TITLE     RanBPM, Muskelin, p48EMLP, p44CTLH, and the armadillo-repeat
            proteins ARMC8alpha and ARMC8beta are components of the CTLH
            complex
  JOURNAL   Gene 396 (2), 236-247 (2007)
   PUBMED   17467196
  REMARK    GeneRIF: RanBPM, ARMC8alpha, ARMC8beta, Muskelin, p48EMLP, and
            p44CTLH form complexes in cells.
REFERENCE   7  (residues 1 to 391)
  AUTHORS   Bowzard JB, Cheng D, Peng J and Kahn RA.
  TITLE     ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs
  JOURNAL   J. Biol. Chem. 282 (24), 17568-17580 (2007)
   PUBMED   17452337
REFERENCE   8  (residues 1 to 391)
  AUTHORS   Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A,
            Meil A, Wojcik J, Legrain P and Gauthier JM.
  TITLE     Functional proteomics mapping of a human signaling pathway
  JOURNAL   Genome Res. 14 (7), 1324-1332 (2004)
   PUBMED   15231748
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AK023972.1, BC047668.1, BC012165.1, AC064848.5 and BU620245.1.
            
            Sequence Note: The RefSeq transcript and protein were derived from
            transcript and genomic sequence to make the sequence consistent
            with the reference genome assembly. The genomic coordinates used
            for the transcript record were based on alignments.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803616.90910.1,
                                           SRR1660805.158266.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..391
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="2"
                     /map="2p11.2"
     Protein         1..391
                     /product="E3 ubiquitin-protein transferase RMND5A"
                     /EC_number="2.3.2.27"
                     /note="C-terminal to LisH motif, 44 kDa; protein RMD5
                     homolog A; GID complex subunit 2 homolog A; 44-kD protein
                     coding for CTLH motif"
                     /calculated_mol_wt=43862
     Site            1
                     /site_type="other"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="N-acetylmethionine. {ECO:0000244|PubMed:22814378};
                     propagated from UniProtKB/Swiss-Prot (Q9H871.1)"
     Region          114..146
                     /region_name="LisH"
                     /note="Lissencephaly type-1-like homology motif;
                     smart00667"
                     /db_xref="CDD:128913"
     Region          153..297
                     /region_name="CLTH"
                     /note="CTLH/CRA C-terminal to LisH motif domain;
                     pfam10607"
                     /db_xref="CDD:313761"
     Region          333..381
                     /region_name="dRING_RMD5A"
                     /note="Degenerated RING finger found in protein RMD5
                     homolog A (RMD5A); cd16794"
                     /db_xref="CDD:319708"
     Region          336..377
                     /region_name="degenerated RING finger"
                     /note="degenerated RING finger [structural motif]"
                     /db_xref="CDD:319708"
     CDS             1..391
                     /gene="RMND5A"
                     /gene_synonym="CTLH; GID2; GID2A; p44CTLH; RMD5"
                     /coded_by="NM_022780.4:378..1553"
                     /db_xref="CCDS:CCDS1991.1"
                     /db_xref="GeneID:64795"
                     /db_xref="HGNC:HGNC:25850"
ORIGIN      
        1 mdqcvtvere lekvlhkfsg ygqlcergle elidytgglk heilqshgqd aelsgtlslv
       61 ltqcckrikd tvqklasdhk dihssvsrvg kaidknfdsd issvgidgcw qadsqrllne
      121 vmvehffrqg mldvaeelcq esglsvdpsq kepfvelnri lealkvrvlr palewavsnr
      181 emliaqnssl efklhrlyfi sllmggttnq realqyaknf qpfalnhqkd iqvlmgslvy
      241 lrqgienspy vhlldanqwa dicdiftrda callglsves plsvsfsagc valpalinik
      301 avieqrqctg vwnqkdelpi evdlgkkcwy hsifacpilr qqttdnnppm klvcghiisr
      361 dalnkmfngs klkcpycpme qspgdakqif f
//

1. (RMD5A)